The Effects of Batch Ceh-Ms Mode on the Umami Profile of Chicken Breast Enzymatic Hydrolysate and the Taste Mechanism of Umami Peptides

Abstract

The present study further explored the effect of batch coupled enzymatic hydrolysis and membrane separation (CEH-MS) mode and traditional EH (enzymatic hydrolysis) and offline MS (membrane separation) mode on the umami intensity of enzymatic hydrolysate of chicken breast and focus extended to unraveling the umami mechanism of peptide presentation, commencing with enhancements in enzymatic efficiency. An amino acid analyzer was employed for the analysis of amino acids, while high-performance liquid chromatography was utilized to determine organic acids and nucleotides. Prediction of peptides’ umami utilized umami_YYDS and BIOPEP-UWM. Molecular docking elucidated the binding mechanism of umami peptides to T1R1/T1R3. Crucial amino acid residues implicated in this binding included Asn68, His145, Ser146, Glu172, Ser177, Tyr182, Glu217, Arg220, Asp249, Val277, Ala302, Asp364, Gln389, among others.

Keywords: Batch CEH-MS mode, Traditional EH and offline MS mode, Chicken breast, Umami, Molecular docking